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Preliminary X‐ray diffraction analysis of a thermophilic β‐1,3–1,4‐glucanase from Clostridium thermocellum
Author(s) -
Zhang Lilan,
Zhao Puya,
Chen ChunChi,
Huang ChunHsiang,
Ko TzuPing,
Zheng Yingying,
Guo ReyTing
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14009376
Subject(s) - clostridium thermocellum , thermophile , microbiology and biotechnology , glucanase , chemistry , biology , bacteria , cellulase , organic chemistry , enzyme , genetics
β‐1,3–1,4‐Glucanases catalyze the specific hydrolysis of internal β‐1,4‐glycosidic bonds adjacent to the 3‐ O ‐substituted glucose residues in mixed‐linked β‐glucans. The thermophilic glycoside hydrolase CtGlu16A from Clostridium thermocellum exhibits superior thermal profiles, high specific activity and broad pH adaptability. Here, the catalytic domain of CtGlu16A was expressed in Escherichia coli , purified and crystallized in the trigonal space group P 3 1 21, with unit‐cell parameters a = b = 74.5, c = 182.9 Å, by the sitting‐drop vapour‐diffusion method and diffracted to 1.95 Å resolution. The crystal contains two protein molecules in an asymmetric unit. Further structural determination and refinement are in progress.